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Database: UniProt
Entry: A0A0C5VL11_9GAMM
LinkDB: A0A0C5VL11_9GAMM
Original site: A0A0C5VL11_9GAMM 
ID   A0A0C5VL11_9GAMM        Unreviewed;       485 AA.
AC   A0A0C5VL11;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 38.
DE   RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361160};
DE            EC=1.2.1.- {ECO:0000256|RuleBase:RU361160};
GN   ORFNames=YC6258_02962 {ECO:0000313|EMBL:AJQ95001.1};
OS   Gynuella sunshinyii YC6258.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Saccharospirillaceae; Gynuella.
OX   NCBI_TaxID=1445510 {ECO:0000313|EMBL:AJQ95001.1, ECO:0000313|Proteomes:UP000032266};
RN   [1] {ECO:0000313|EMBL:AJQ95001.1, ECO:0000313|Proteomes:UP000032266}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YC6258 {ECO:0000313|EMBL:AJQ95001.1,
RC   ECO:0000313|Proteomes:UP000032266};
RA   Khan H., Chung E.J., Chung Y.R.;
RT   "Full genme sequencing of cellulolytic bacterium Gynuella sunshinyii
RT   YC6258T gen. nov., sp. nov.";
RL   Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase
CC       family. {ECO:0000256|ARBA:ARBA00007406, ECO:0000256|RuleBase:RU000397}.
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DR   EMBL; CP007142; AJQ95001.1; -; Genomic_DNA.
DR   RefSeq; WP_044620021.1; NZ_CP007142.1.
DR   AlphaFoldDB; A0A0C5VL11; -.
DR   STRING; 1445510.YC6258_02962; -.
DR   KEGG; gsn:YC6258_02962; -.
DR   PATRIC; fig|1445510.3.peg.2932; -.
DR   HOGENOM; CLU_030140_1_2_6; -.
DR   OrthoDB; 9803304at2; -.
DR   Proteomes; UP000032266; Chromosome.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR   GO; GO:0016620; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR   GO; GO:0006006; P:glucose metabolic process; IEA:InterPro.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR020831; GlycerAld/Erythrose_P_DH.
DR   InterPro; IPR020830; GlycerAld_3-P_DH_AS.
DR   InterPro; IPR020829; GlycerAld_3-P_DH_cat.
DR   InterPro; IPR020828; GlycerAld_3-P_DH_NAD(P)-bd.
DR   InterPro; IPR006424; Glyceraldehyde-3-P_DH_1.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   NCBIfam; TIGR01534; GAPDH-I; 1.
DR   PANTHER; PTHR43454; GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE; 1.
DR   PANTHER; PTHR43454:SF1; GP_DH_N DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF02800; Gp_dh_C; 1.
DR   Pfam; PF00044; Gp_dh_N; 1.
DR   PRINTS; PR00078; G3PDHDRGNASE.
DR   SMART; SM00846; Gp_dh_N; 1.
DR   SUPFAM; SSF55347; Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00071; GAPDH; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU361160};
KW   Reference proteome {ECO:0000313|Proteomes:UP000032266}.
FT   DOMAIN          135..296
FT                   /note="Glyceraldehyde 3-phosphate dehydrogenase NAD(P)
FT                   binding"
FT                   /evidence="ECO:0000259|SMART:SM00846"
SQ   SEQUENCE   485 AA;  53676 MW;  6ECBBAF0A4CA4555 CRC64;
     MVSIINAQKQ LSEWQEKEAL LEQMIPLIGR LYRHNNVITS IYGRSVINQS VINLVKSHRF
     VRQTEGHELE PSDTLAILKV LDALNLGPCH IDIGKLAIAY REYQETPLSD WLRSQLSEVV
     NQYHQNNSDQ TARRKDVVLY GFGRIGRFLA RILVEKSGGS PLALRAIVVR KSGAANDLVK
     RASLLRRDSI HGSFEGTISI DEENNAIIAN GSYIQVIYAN SPAEVDYTKY GIENALVIDN
     TGVWRDEKGL SQHLQSKGVG KVLLTAPGKG DLKNIVYGIN HNTIEESDRI VSAASCTTNA
     ITPVLKVIND TFGIQHGHVE TIHSYTNDQN LIDNFHKGDR RGRSAPLNMV VTETGAAKAV
     AKALPELNGK LTGNAIRVPT PNVSLAILNL DLLKPVSRDS LNEMLRERSL YSELNKQIDF
     VNSPDAVSSD FVGNRRAGIV DAKATIVSGH KAILYVWYDN EAGYSAQVMR LVQKMAGIEY
     RFFPA
//
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